ID A0A117RRZ3_9ACTN Unreviewed; 724 AA.
AC A0A117RRZ3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=AQJ67_04175 {ECO:0000313|EMBL:KUO06007.1};
OS Streptomyces caeruleatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=661399 {ECO:0000313|EMBL:KUO06007.1, ECO:0000313|Proteomes:UP000053429};
RN [1] {ECO:0000313|EMBL:KUO06007.1, ECO:0000313|Proteomes:UP000053429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24802 {ECO:0000313|EMBL:KUO06007.1,
RC ECO:0000313|Proteomes:UP000053429};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces caeruleatus NRRL B-24802, type
RT strain for the species Streptomyces caeruleatus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000256|ARBA:ARBA00008465}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUO06007.1}.
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DR EMBL; LMWY01000003; KUO06007.1; -; Genomic_DNA.
DR RefSeq; WP_062716572.1; NZ_KQ948924.1.
DR AlphaFoldDB; A0A117RRZ3; -.
DR STRING; 661399.AQJ67_04175; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000053429; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
DR CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR CDD; cd03679; MM_CoA_mutase_alpha_like; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR InterPro; IPR006098; MMCoA_mutase_a_cat.
DR NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR NCBIfam; TIGR00641; acid_CoA_mut_N; 1.
DR PANTHER; PTHR48101:SF4; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KUO06007.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053429}.
FT DOMAIN 591..723
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 78554 MW; 7520B71A13C34BDE CRC64;
MGIPDFSGIE LGTPATGGGA DEWRTAVKQA TGGDEPLWET PEGIAVKPLY TGRDLEGLDF
LGTYPGMAPY LRGPYPTMYV NQPWTIRQYA GFSTAEESNA FYRRNLAAGQ KGLSVAFDLP
THRGYDSDHP RVTGDVGMAG VAIDSIYDMR QLFDGIPLDK MTVSMTMNGA VLPVLALYIV
AAEEQGVPPE KLAGTIQNDI LKEFMVRNTY IYPPKPSMRI ISDIFAFTSQ RMPRYNSISI
SGYHIQEAGA TADLELAYTL ADGVEYIRAG REAGLDVDAF APRLSFFWAI GMNFFMEVAK
LRAARLLWAK LVKQFDPKNS KSLSLRTHSQ TSGWSLTAQD VFNNVTRTCV EAMAATQGHT
QSLHTNALDE ALALPTDFSA RIARNTQLLL QQESGTTRVI DPWGGSAYVE KLTYDLARRA
WQHIQEVEAA GGMAKAIDAG LPKLRIEEAA ARTQARIDSG RQPVIGVNKY RVDSDEQIDV
LKVDNSSVRA QQIAKLRRLR EERDETACRD ALDALTRAAG GEGNLLELAV NAARAKATVG
EISDALEKVY GRHASQIRTI SGVYRNEAGE SPSVDRTRTL VDSFEESEGR RPRILVAKMG
QDGHDRGQKV IATAFADLGF DVDVGPLFQT PAEVARQAVE ADVHIVGVSS LAAGHLTLVP
ALKEALAEEG REDIMIVVGG VIPPQDVATL LEMGAAAVFP PGTVIPDAAH DLVERLAADL
GHGV
//
